ID A0A2Z6IAV9_9BURK Unreviewed; 743 AA.
AC A0A2Z6IAV9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SUTMEG_15540 {ECO:0000313|EMBL:BBF23663.1};
OS Sutterella megalosphaeroides.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF23663.1, ECO:0000313|Proteomes:UP000271003};
RN [1] {ECO:0000313|EMBL:BBF23663.1, ECO:0000313|Proteomes:UP000271003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF23663.1,
RC ECO:0000313|Proteomes:UP000271003};
RX PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT human faeces.";
RL Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; AP018786; BBF23663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6IAV9; -.
DR KEGG; sutt:SUTMEG_15540; -.
DR Proteomes; UP000271003; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12974; Phosphonate-bd; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000271003};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 449..662
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 681..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 81352 MW; 743FC5E14E1ECD45 CRC64;
MGTTTGTPSS DIRAAIRPDM AEIPEPEAIK NAKISADALV GVPVISERMR IGRPIRIGIE
AELGRTQYAS WIRYTLEALR HALGKKNVQV FYLDGRGLSV ALQNSEIDFF IANSHTFALQ
QSKTTVEQLA TFLPVDALRA EEAQAGVLFM KKGALEGNML ARNDAGGSTS ATTVATQRAV
TSDGTATVFT STGSRVSERQ NLQHLIESLK EGGIVAVERT SLGGWLAPLA LLQREGLSAQ
AAGRRTTFTN GDERAVLDAV LSGEAVLGIL PACSLERFQE AGVVDVKRDL VIVDPQLADG
LACAHSTPTY PGWAFGTTAK TDPLLKKNIG SLLFSMNADR YGGQWQFPAL NRSIYDLFYE
LKMGPYEHLA TWSLHRFMRE NSEALALIIF LTFVVISYAV SLSVLVRRKT QQLRDALHDR
DLVEAEAAQS RQHIANLERT GIVGQMSTII AHELKQPLSA ISNYANSLHR RTKNDKFDKE
SFIWALTEIA NEAERASRIV DRVRSYAKHD YPPRTVTDLS VVIGNSITTF RRSRQTNAEI
VVRVNPGSMA EVDAWEIELA VLNLLKNAAD AISGVEKPRI EVSLVARDAK TWALSVGDNG
PYISDEQLAL FFKPLQTTKG AKGMGLGLSI VANIAERHAG RVTVERNGTA GVRFTITFPR
LPGETEKPIE DAMLPPRMTV YEGNPKPAKS AGMLDAQIRS EVDRAAERDH PSERSDRTPG
EDTPVTIHSR GFSRMLDRLE GKS
//